Structure of PDB 6ck6 Chain A

Receptor sequence
>6ck6A (length=271) Species: 9606 (Homo sapiens) [Search protein sequence]
GSTDSFSGRFEDVYQLQEDVLGEGAHARVQTCINLITSQEYAVKIIEKQP
GHIRSRVFREVEMLYQCQGHRNVLELIEFFEEEDRFYLVFEKMRGGSILS
HIHKRRHFNELEASVVVQDVASALDFLHNKGIAHRDLKPENILCEHPNQV
SPVKICDFGGSAEYMAPEVVEAFSEEASIYDKRCDLWSLGVILYILLSGY
PPFVGRCCGACPACQNMLFESIQEGKYEFPDKDWAHISCAAKDLISKLLV
RDAKQRLSAAQVLQHPWVQGC
3D structure
PDB6ck6 Structure-based Design of Pyridone-Aminal eFT508 Targeting Dysregulated Translation by Selective Mitogen-activated Protein Kinase Interacting Kinases 1 and 2 (MNK1/2) Inhibition.
ChainA
Resolution3.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D205 K207 N210 D226 S253
Catalytic site (residue number reindexed from 1) D136 K138 N141 D157 S161
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN A C299 C311 C207 C211
BS02 N45 A L90 K113 F159 M162 G165 N210 L212 C225 D226 L21 K44 F90 M93 G96 N141 L143 C156 D157 PDBbind-CN: -logKd/Ki=9.00,IC50=1.0nM
BindingDB: IC50=1.000000nM,Ki=3.0nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6ck6, PDBe:6ck6, PDBj:6ck6
PDBsum6ck6
PubMed29526098
UniProtQ9HBH9|MKNK2_HUMAN MAP kinase-interacting serine/threonine-protein kinase 2 (Gene Name=MKNK2)

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